Characterization of MiFUT11 from Mangifera indica L.: A functional core α1,3-fucosyltransferase potentially involved in the biosynthesis of immunogenic carbohydrates in mango fruit

Abstract In higher plants, asparagine-linked oligosaccharides(N- glycans) in glycoproteins carry unique carbohydrate epitopes, namely, a core α1,3- fucoseand/or a β1,2-xylose, which are common determinants responsible for the cross-reactivityof plant glycoproteins due to their strong immunogenicity. While these determinants and the relevant genes have been well characterized for herbaceous plants, information concerning whether many food plants cross-react with airborne pollens is not available. In this paper, we report on the characterization of a novel core α1,3- fucosyltransferasegene identified from Mangiferaindica L., one of the major plants potentially related to food allergy. Based on sequence information of plant homologues, we amplified a candidate cDNA (MiFUT11) from pericarp tissue. An in vitro assay demonstrated that the recombinant MiFUT11 protein transfers a fucoseunit onto both non- fucosylatedand core α1,6- fucosylated oligosaccharides. A glycoform analysis using MALDI-TOF mass spectrometry showed that the introduction of the MiFUT11 cDNA increased the production of a core α1,3- and α1,6- fucosylatedpauci-mannosidic oligosaccharidein SpodopteraSf21 cells. Our findings suggest that MiFUT11 is a functional core α1,3- fucosyltransferasegene that is involved in the assembly of cross-reactiveN- glycansin mango fruit.